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C100683200v1
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Papers In Press, published online ahead of print January 3, 2002
J. Biol. Chem, 10.1074/jbc.C100683200
Submitted on November 28, 2001
Revised on January 3, 2002
Accepted on January 3, 2002

The integration of YidC into the cytoplasmic membrane of Escherichia coli requires the signal recognition particle, SecA and SecYEG

Hans Georg Koch, Michael Moser, Karl Ludwig Schimz, and Matthias Müller

Inst. for Biochem. & Mol. Biol., University Freiburg, Freiburg, BW 79104

Corresponding Author: Hans-Georg.Koch{at}biochemie.uni-freiburg.de

The integration of the polytopic membrane protein YidC into the inner membrane of E. coli was analyzed employing an in vitro system. Upon integration of in vitro synthesized YidC, a 42 kDa membrane protected fragment was detected, which could be immuno-precipitated with polyclonal anti-YidC antibodies. The occurrence of this fragment is in agreement with the predicted topology of YidC and probably encompasses the first two transmembrane domains and the connecting 320 amino acid long periplasmic loop. The integration of YidC was strictly dependent on the signal recognition particle (SRP) and SecA. YidC could not be integrated in the absence of SecY, SecE or SecG, suggesting that YidC in contrast to its mitochondrial orthologue Oxa1p,cannot engage a SecYEG-independent protein conducting channel.


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